PAK6-mediated phosphorylation of PPP2R2C regulates LRRK2-PP2A complex formation
PAK6-mediated phosphorylation of PPP2R2C regulates LRRK2-PP2A complex formation
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Author / Creator
Iannotta, Lucia , Emanuele, Marco , Favetta, Giulia , Tombesi, Giulia , Vandewynckel, Laurine , Lara Ordóñez, Antonio Jesús , Saliou, Jean-Michel , Drouyer, Matthieu , Sibran, William , Civiero, Laura , Nichols, R Jeremy , Athanasopoulos, Panagiotis S , Kortholt, Arjan , Chartier-Harlin, Marie-Christine , Greggio, Elisa and Taymans, Jean-Marc
Publisher
Switzerland: Frontiers Research Foundation
Journal title
Language
English
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Publisher
Switzerland: Frontiers Research Foundation
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Scope and Contents
Contents
Mutations in leucine-rich repeat kinase 2 (LRRK2) are a common cause of inherited and sporadic Parkinson's disease (PD) and previous work suggests that dephosphorylation of LRRK2 at a cluster of heterologous phosphosites is associated to disease. We have previously reported subunits of the PP1 and PP2A classes of phosphatases as well as the PAK6 ki...
Alternative Titles
Full title
PAK6-mediated phosphorylation of PPP2R2C regulates LRRK2-PP2A complex formation
Authors, Artists and Contributors
Author / Creator
Emanuele, Marco
Favetta, Giulia
Tombesi, Giulia
Vandewynckel, Laurine
Lara Ordóñez, Antonio Jesús
Saliou, Jean-Michel
Drouyer, Matthieu
Sibran, William
Civiero, Laura
Nichols, R Jeremy
Athanasopoulos, Panagiotis S
Kortholt, Arjan
Chartier-Harlin, Marie-Christine
Greggio, Elisa
Taymans, Jean-Marc
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Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_5c7b59f9a8734bce82374910d2ad476b
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_5c7b59f9a8734bce82374910d2ad476b
Other Identifiers
ISSN
1662-5099
E-ISSN
1662-5099
DOI
10.3389/fnmol.2023.1269387
